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TranscriptomicsThe ER-Associated Degradation Adapter Protein Sel1L Regulates Triglyceride Metabolism via Lipoprotein Lipase
Sel1L is an adaptor protein for the E3 ligase Hrd1 in the endoplasmic reticulum-associated degradation (ERAD), but its physiological role in a cell-type-specific manner remains unclear. Here we show that mice with adipocyte-specific Sel1L deficiency are resistant to diet-induced obesity and exhibit ...
ORGANISM(S): Mus musculus 
2015-05-18 | E-GEOD-56918 | biostudies-arrayexpress
ProteomicsCharacterization of Endoplasmic Reticulum-Associated Degradation in the human fungal pathogen C. albicans
C. albicans is the most prevalent human fungal pathogen. In immunocompromised individuals, C. albicans can cause serious systemic disease and patients infected with drug-resistant isolates have few treatment options. The Ubiquitin-Proteasome System has not been thoroughly characterized in C. albica...
ORGANISM(S): Candida Albicans (ncbitaxon:5476) 
2023-05-03 | MSV000091843 | MassIVE
ProteomicsAn ERAD independent role for rhomboid pseudoprotease Dfm1 in mediating sphingolipid homeostasis
Nearly one-third of nascent proteins are initially targeted to the endoplasmic reticulum (ER) where they are correctly folded and assembled before being delivered to their final cellular destinations. To prevent the accumulation of misfolded membrane proteins, ER-associated-degradation (ERAD) remove...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
MSV000090333 | MassIVE
ProteomicsER-associated degradation ligase HRD1 links ER stress to DNA damage repair by modulating the activity of DNA-PKcs
ER-associated degradation ligase HRD1 links ER stress to DNA damage repair by modulating the activity of DNA-PKcs
ORGANISM(S): Homo Sapiens 
PXD055020 |
GenomicsInduced ubiquitination drives ER protein degradation through a VCP-dependent pathway
Induced ubiquitination drives ER protein degradation through a VCP-dependent pathway
PRJNA1530958 | ENA
TranscriptomicsIRE1alpha is an endogenous substrate of endoplasmic reticulum-associated degradation
Endoplasmic reticulum-associated degradation (ERAD) represents a principle quality control (QC) mechanism to clear misfolded proteins in the ER; however, its physiological significance and the nature of endogenous ERAD substrates remain largely unknown. Here we discover that IRE1alpha, the sensor of...
ORGANISM(S): Mus musculus 
2015-11-04 | E-GEOD-70563 | biostudies-arrayexpress
ProteomicsER-stress-induced_transcription
A conserved AAA+ ATPase network regulates ER-stress-induced transcription
ORGANISM(S): Caenorhabditis Elegans (c. Elegans) 
2015-12-31 | PAe005594 | PeptideAtlas
MetabolomicsIdentifying metabolic alterations associated with coral growth anomalies using 1H NMR metabolomics
Coral growth anomalies (GAs) are tumor-like protrusions that are detrimental to coral health, impacting both the coral skeleton and soft tissues. These lesions are increasingly found throughout the tropics and are commonly associated with high human population density, yet little is known about the ...
2021-06-15 | MTBLS2424 | MetaboLights
ProteomicsProinsulin degradation and presentation of a proinsulin B-chain autoantigen involves ER-associated protein degradation (ERAD)-enzyme UBE2G2
Type 1 diabetes (T1D) is characterized by HLA class I-mediated presentation of autoantigens on the surface of pancreatic β-cells. Recognition of these autoantigens by CD8¬¬+ T cells results in the destruction of pancreatic β-cells and, consequently, insulin deficiency. Most epitopes presented at the...
ORGANISM(S): Homo sapiens (Human) 
2024-03-20 | PXD049996 | Pride
Ube2g2 Type 1 diabetes Insulin-derived peptides Proinsulin Hla-class i 
TranscriptomicsUnfolded Protein Response
To dissect the requirements of membrane protein degradation from the ER, we expressed the mouse major histocompatibility complex class I heavy chain H-2K(b) in yeast. Like other proteins degraded from the ER, unassembled H-2K(b) heavy chains are not transported to the Golgi but are degraded in a pro...
ORGANISM(S): Saccharomyces cerevisiae 
2005-08-16 | E-GEOD-3130 | biostudies-arrayexpress
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